The Taenia crassiceps recombinant
antigen KETc7 has been shown to be effective as a
vaccine against experimental murine
cysticercosis, a laboratory model used to test potentially promising molecules against porcine
Taenia solium cysticercosis. Based on the deduced amino acid sequence of this
proline-rich
polypeptide, three fragments, GK-1, GK-2, and GK-3, were chemically synthesized in linear form. Of the three
peptides, only GK-1 induced sterile protection against T. crassiceps
cysticercosis in 40 to 70% of BALB/cAnN male mice. GK-1 is an 18-amino-acid
peptide which contains at least one
B-cell epitope, as demonstrated by its ability to induce an antibody response to the
peptide and T. crassiceps
antigen without need of a
carrier protein. Immunofluorescence studies revealed that anti-GK1
antibodies strongly react with the native
protein in the tegument of T. crassiceps and also with anatomical structures of T. solium eggs, oncospheres, cysticercus, and tapeworm. GK-1 also contains at least one
T-cell epitope, capable of stimulating the proliferation of CD8(+) and to a lower extent CD4(+) T cells primed either with the free
peptide or T. crassiceps total
antigen. The supernatant of the stimulated cells contained high levels of
gamma interferon and low levels of
interleukin-4. Similar results were obtained with T cells tested for intracellular
cytokine production, an indication of the
peptide's capacity to induce an inflammatory response. The remarkable protection induced by GK-1 immunization, its physicochemical properties, and its presence in all developmental stages of T. solium point to this synthetic
peptide as a strong candidate in the construction of a
synthetic vaccine against T. solium pig
cysticercosis.